A method for improving the hydrogen-deuterium atom exchange efficiency of protein in deuterated reagent

Abstract

The invention provides a method for improving hydrogen and deuterium atomic exchanging efficiency of protein in nuclear magnetism reagent by pressurizing inert gas and radiating isotopes under an anaerobic condition. The to-be-detected protein is dissolved in the nuclear magnetism reagent, and inert gas is introduced into a solution system so as to increase the pressure to 0.15MPa to 1.0MPa. The radioactive source selects radioactive isotopes such as cobalt-60 and caesium-137, and the dosage is 5kGy to 500kGy. The detected protein basically contains all protein types, and the exchanging rate is detected in a mass-spectrography.

Description

technical field

[0001] The invention relates to a method for increasing the hydrogen-deuterium atom exchange efficiency of proteins in deuterated reagents by using pressurization under anaerobic state and isotope radiation to provide additional energy. The invention belongs to the field of chemical reaction thermodynamics. Background technique

[0002] Proteins in their natural state generally have a tightly folded structure. The α-position hydrogen atoms on the amino acid backbone of the protein are in different spatial positions due to folding or helical conformation. Under anaerobic conditions, radioactive isotopes can be irradiated to trigger the transfer of the α-position hydrogen atoms of amino acid fragments to form α-carbon free radical centers. At the same time, in a certain probability, if the α-side chain terminal of the amino acid fragment also contains hydrogen atoms, similarly, an α-position side chain free radical center can also be formed at the α-position ...